메뉴 건너뛰기




Volumn 68, Issue 7, 2000, Pages 3990-3997

Inhibitory and bactericidal effects of hydrogen peroxide production by Streptococcus pneumoniae on other inhabitants of the upper respiratory tract

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; HYDROGEN PEROXIDE; PYRUVATE OXIDASE;

EID: 0033945724     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.68.7.3990-3997.2000     Document Type: Article
Times cited : (283)

References (52)
  • 2
    • 0343162669 scopus 로고
    • Hydrogen peroxide accumulation during growth of the pneumococcus
    • Annear, D. I., and D. C. Dorman. 1952. Hydrogen peroxide accumulation during growth of the pneumococcus. Aust. J. Exp. Bio. Med. Sci. 30:191-195.
    • (1952) Aust. J. Exp. Bio. Med. Sci. , vol.30 , pp. 191-195
    • Annear, D.I.1    Dorman, A.D.C.2
  • 4
    • 84983711696 scopus 로고
    • Studies on the nature of the chemical nature of the substance inducing transformation of pneumococcal types
    • Avery, O. T., C. M. MacLeod, and M. McCarty. 1944. Studies on the nature of the chemical nature of the substance inducing transformation of pneumococcal types. J. Exp. Med. 79:137-157.
    • (1944) J. Exp. Med. , vol.79 , pp. 137-157
    • Avery, O.T.1    MacLeod, C.M.2    McCarty, M.3
  • 5
    • 0029757332 scopus 로고    scopus 로고
    • The alpha-hemolysin of Streptococcus gordonii is hydrogen peroxide
    • Barnard, J. P., and M. W. Stinson. 1996. The alpha-hemolysin of Streptococcus gordonii is hydrogen peroxide. Infect. Immun. 64:3853-3857.
    • (1996) Infect. Immun. , vol.64 , pp. 3853-3857
    • Barnard, J.P.1    Stinson, A.M.W.2
  • 6
    • 0029741480 scopus 로고    scopus 로고
    • Cloning and characterization of nanB, a second Streptococcus pneumoniae neuraminidase gene, and purification of the NanB enzyme from recombinant Escherichia coli
    • Berry, A., R. Lock, and J. Paton. 1996. Cloning and characterization of nanB, a second Streptococcus pneumoniae neuraminidase gene, and purification of the NanB enzyme from recombinant Escherichia coli. J. Bacteriol. 178:4854-4860.
    • (1996) J. Bacteriol. , vol.178 , pp. 4854-4860
    • Berry, A.1    Lock, R.2    Paton, J.3
  • 7
    • 0021612174 scopus 로고
    • Quantitative determination of catalase activity produced by Neisseria gonorrhoeae, Staphylococcus epidermidis. Neisseria meningitidis, and other bacterial strains using the Catalasemeter
    • Bisaillon, J., G. Dubois, R. Beaudet, M. Sylvestre, R. Charbonneau, and M. Gagnon. 1985. Quantitative determination of catalase activity produced by Neisseria gonorrhoeae, Staphylococcus epidermidis. Neisseria meningitidis, and other bacterial strains using the Catalasemeter. Exp. Biol. 43:225-230.
    • (1985) Exp. Biol. , vol.43 , pp. 225-230
    • Bisaillon, J.1    Dubois, G.2    Beaudet, R.3    Sylvestre, M.4    Charbonneau, R.5    Gagnon, M.6
  • 8
    • 0028043692 scopus 로고
    • Characterization and virulence analysis of catalase mutants of Haemophilus influenzae
    • Bishai, W., N. Howard, J. Winkelstein, and H. Smith. 1994. Characterization and virulence analysis of catalase mutants of Haemophilus influenzae. Infect. Immun. 62:4855-60.
    • (1994) Infect. Immun. , vol.62 , pp. 4855-4860
    • Bishai, W.1    Howard, N.2    Winkelstein, J.3    Smith, H.4
  • 9
    • 0019427933 scopus 로고
    • Antiphosphocholine antibodies found in normal mouse serum are protective against intravenous infection with type 3 Streptococcus pneumoniae
    • Briles, D. E., M. Nahm, K. Schroer, J. Davie, P. Baker, J. Kearney, and R. Barletta. 1981. Antiphosphocholine antibodies found in normal mouse serum are protective against intravenous infection with type 3 Streptococcus pneumoniae. J. Exp. Med. 153:694-705.
    • (1981) J. Exp. Med. , vol.153 , pp. 694-705
    • Briles, D.E.1    Nahm, M.2    Schroer, K.3    Davie, J.4    Baker, P.5    Kearney, J.6    Barletta, R.7
  • 10
    • 0027999183 scopus 로고
    • A neuraminidase from Streptococcus pneumoniae has the features of a surface protein
    • Camara, M., G. J. Boulnois, P. W. Andrew, and T. J. Mitchell. 1994. A neuraminidase from Streptococcus pneumoniae has the features of a surface protein. Infect. Immun. 62:3688-3695.
    • (1994) Infect. Immun. , vol.62 , pp. 3688-3695
    • Camara, M.1    Boulnois, G.J.2    Andrew, P.W.3    Mitchell, T.J.4
  • 11
    • 0342293026 scopus 로고
    • Bacterial antagonism, with particular reference to meningococcus
    • Colebrook, L. 1915. Bacterial antagonism, with particular reference to meningococcus. Lancet ii:1136-1138.
    • (1915) Lancet , vol.2 , pp. 1136-1138
    • Colebrook, L.1
  • 12
    • 0029165459 scopus 로고
    • Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor
    • Cundell, D. R., N. P. Gerard, C. Gerard, I. Idanpaan-Heikkila, and E. I. Tuomanen. 1995. Streptococcus pneumoniae anchor to activated human cells by the receptor for platelet-activating factor. Nature 377:435-438.
    • (1995) Nature , vol.377 , pp. 435-438
    • Cundell, D.R.1    Gerard, N.P.2    Gerard, C.3    Idanpaan-Heikkila, I.4    Tuomanen, E.I.5
  • 13
    • 85010250943 scopus 로고
    • Hydrogen peroxide formation by lactobacilli and its effect on Staphylococcus aureus
    • Dahiya, R. S., and M. L. Speck. 1968. Hydrogen peroxide formation by lactobacilli and its effect on Staphylococcus aureus. J. Dairy Sci. 51:1568-1572.
    • (1968) J. Dairy Sci. , vol.51 , pp. 1568-1572
    • Dahiya, R.S.1    Speck, M.L.2
  • 15
    • 0027377225 scopus 로고
    • Identification of hydrogen peroxide as a Streptococcus pneumoniae toxin for rat alveolar epithelial cells
    • Duane, P. G., J. B. Rubins, H. R. Weisel, and E. N. Janoff. 1993. Identification of hydrogen peroxide as a Streptococcus pneumoniae toxin for rat alveolar epithelial cells. Infect. Immun. 61:4392-4397.
    • (1993) Infect. Immun. , vol.61 , pp. 4392-4397
    • Duane, P.G.1    Rubins, J.B.2    Weisel, H.R.3    Janoff, E.N.4
  • 16
    • 0021254125 scopus 로고
    • Inhibition of Neisseria gonorrhoeae growth due to hydrogen peroxide production by urogenital streptococci
    • Dubreuil, D., J. G. Bisaillon, and R. Beaudet. 1984. Inhibition of Neisseria gonorrhoeae growth due to hydrogen peroxide production by urogenital streptococci. Microbios 39:159-167.
    • (1984) Microbios , vol.39 , pp. 159-167
    • Dubreuil, D.1    Bisaillon, J.G.2    Beaudet, R.3
  • 17
    • 1842299263 scopus 로고    scopus 로고
    • Sialylation of Neisseria meningitidis lipooligosaccharide inhibits serum bactericidal activity masking lacto-N-neotraose
    • Estabrook, M. M., J. M. Griffiss, and G. A. Jarvis. 1997. Sialylation of Neisseria meningitidis lipooligosaccharide inhibits serum bactericidal activity masking lacto-N-neotraose. Infect. Immun. 65:4436-4444.
    • (1997) Infect. Immun. , vol.65 , pp. 4436-4444
    • Estabrook, M.M.1    Griffiss, J.M.2    Jarvis, G.A.3
  • 19
    • 0033976512 scopus 로고    scopus 로고
    • Relative roles of pneumolysin and hydrogen peroxide from Streptococcus pneumoniae in inhibition of ependymal ciliary beat frequency
    • Hirst, R. A., K. S. Sikand, A. Rutman, T. J. Mitchell, P. W. Andrew, and C. O'Callaghan. 2000. Relative roles of pneumolysin and hydrogen peroxide from Streptococcus pneumoniae in inhibition of ependymal ciliary beat frequency. Infect. Immun. 68:1557-1562.
    • (2000) Infect. Immun. , vol.68 , pp. 1557-1562
    • Hirst, R.A.1    Sikand, K.S.2    Rutman, A.3    Mitchell, T.J.4    Andrew, P.W.5    O'Callaghan, C.6
  • 20
    • 0342293025 scopus 로고
    • The culture of Streptococcus pneumoniae
    • Holt, L. B. 1962. The culture of Streptococcus pneumoniae. J. Gen. Microbiol. 27:327-330.
    • (1962) J. Gen. Microbiol. , vol.27 , pp. 327-330
    • Holt, L.B.1
  • 21
    • 0032773667 scopus 로고    scopus 로고
    • Sialic acid in the lipopolysaccharide of Haemophilus influenzae: Strain distribution, influence on serum resistance and structural characterization
    • Hood, D. W., K. Makepeace, M. E. Deadman, R. F. Rest, P. Thibault, A. Martin, J. C. Richards, and E. R. Moxon. 1999. Sialic acid in the lipopolysaccharide of Haemophilus influenzae: strain distribution, influence on serum resistance and structural characterization. Mol. Microbiol. 33:679-692.
    • (1999) Mol. Microbiol. , vol.33 , pp. 679-692
    • Hood, D.W.1    Makepeace, K.2    Deadman, M.E.3    Rest, R.F.4    Thibault, P.5    Martin, A.6    Richards, J.C.7    Moxon, E.R.8
  • 22
    • 0032900987 scopus 로고    scopus 로고
    • Relationship between cell-surface carbohydrates and intrastrain variation on opsonophagocytosis of Streptococcus pneumoniae
    • Kim, J. O., S. Romero-Steiner, U. Sørensen, J. Blom, M. Carvalho, S. Barnardi, G. Carlone, and J. N. Weiser. 1999. Relationship between cell-surface carbohydrates and intrastrain variation on opsonophagocytosis of Streptococcus pneumoniae. Infect. Immun. 67:2327-2333.
    • (1999) Infect. Immun. , vol.67 , pp. 2327-2333
    • Kim, J.O.1    Romero-Steiner, S.2    Sørensen, U.3    Blom, J.4    Carvalho, M.5    Barnardi, S.6    Carlone, G.7    Weiser, J.N.8
  • 23
    • 0031041922 scopus 로고    scopus 로고
    • Role of nontypeable Haemophilus influenzae in pediatric respiratory tract infections
    • Klein, J. O. 1997. Role of nontypeable Haemophilus influenzae in pediatric respiratory tract infections. Pediatr. Infect. Dis. 16:S5-S8.
    • (1997) Pediatr. Infect. Dis. , vol.16
    • Klein, J.O.1
  • 25
    • 0020053097 scopus 로고
    • Streptococcus pneumoniae and Haemophilus influenzae in nasal cultures during acute otitis media
    • Luotonen, J. 1982. Streptococcus pneumoniae and Haemophilus influenzae in nasal cultures during acute otitis media. Acta Otolaryngol. 93:295-299.
    • (1982) Acta Otolaryngol. , vol.93 , pp. 295-299
    • Luotonen, J.1
  • 26
    • 0033977680 scopus 로고    scopus 로고
    • The position of phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae affects binding and sensitivity to C-reactive protein mediated killing
    • Lysenko, E. S., J. C. Richards, A. D. Cox, A. Stewart, A. Martin, M. Kapoor, and J. N. Weiser. 2000. The position of phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae affects binding and sensitivity to C-reactive protein mediated killing. Mol. Microbiol. 35:234-245.
    • (2000) Mol. Microbiol. , vol.35 , pp. 234-245
    • Lysenko, E.S.1    Richards, J.C.2    Cox, A.D.3    Stewart, A.4    Martin, A.5    Kapoor, M.6    Weiser, J.N.7
  • 27
    • 0029907767 scopus 로고    scopus 로고
    • Lack of expression of the global regulator OxyR in Haemophilus influenzae has a profound effect on growth phenotype
    • MacIver, I., and E. J. Hansen. 1996. Lack of expression of the global regulator OxyR in Haemophilus influenzae has a profound effect on growth phenotype. Infect. Immun. 64:4618-4629.
    • (1996) Infect. Immun. , vol.64 , pp. 4618-4629
    • MacIver, I.1    Hansen, E.J.2
  • 30
    • 0000407950 scopus 로고
    • Pathogenic bacteria in chronic bronchitis
    • May, R. J. 1954. Pathogenic bacteria in chronic bronchitis. Lancet ii:839-842.
    • (1954) Lancet , vol.2 , pp. 839-842
    • May, R.J.1
  • 31
    • 0021752918 scopus 로고
    • Blood clearance by anti-phosphocholine antibodies as a mechanism of protection in experimental pneumococcal bacteremia
    • McDaniel, L. S., W. H. J. Benjamin, C. Forman, and D. E. Briles. 1984. Blood clearance by anti-phosphocholine antibodies as a mechanism of protection in experimental pneumococcal bacteremia. J. Immunol. 133:3308-12.
    • (1984) J. Immunol. , vol.133 , pp. 3308-3312
    • McDaniel, L.S.1    Benjamin, W.H.J.2    Forman, C.3    Briles, D.E.4
  • 32
    • 0026092316 scopus 로고
    • Point mutation in meningococcal porA gene associated with increased endemic disease
    • McGuinness, B., I. Clarke, P. Lambden, A. Barlow, J. Poolman, D. Jones, and J. Heckels. 1991. Point mutation in meningococcal porA gene associated with increased endemic disease. Lancet 337:514-517.
    • (1991) Lancet , vol.337 , pp. 514-517
    • McGuinness, B.1    Clarke, I.2    Lambden, P.3    Barlow, A.4    Poolman, J.5    Jones, D.6    Heckels, J.7
  • 33
    • 0342728057 scopus 로고
    • Catalase production and sensitiveness to hydrogen peroxide amongst bacteria: With a scheme of classification based on these properties
    • McLeod, J. W., and J. Gordon. 1923. Catalase production and sensitiveness to hydrogen peroxide amongst bacteria: with a scheme of classification based on these properties. J. Pathol. Bacteriol. 26:326-331.
    • (1923) J. Pathol. Bacteriol. , vol.26 , pp. 326-331
    • McLeod, J.W.1    Gordon, J.2
  • 34
    • 0003376767 scopus 로고
    • Production of hydrogen peroxide by bacteria
    • McLeod, J. W., and J. Gordon. 1922. Production of hydrogen peroxide by bacteria. Biochem. J. 16:499-506.
    • (1922) Biochem. J. , vol.16 , pp. 499-506
    • McLeod, J.W.1    Gordon, J.2
  • 35
    • 0014961281 scopus 로고
    • Choline-containing teichoic acid as a structural component of pneumococcal cell wall and its role in sensitivity to lysis by an enzyme
    • Mosser, J. L., and A. Tomasz. 1970. Choline-containing teichoic acid as a structural component of pneumococcal cell wall and its role in sensitivity to lysis by an enzyme. J. Biol. Chem. 245:287-298.
    • (1970) J. Biol. Chem. , vol.245 , pp. 287-298
    • Mosser, J.L.1    Tomasz, A.2
  • 36
    • 0019140628 scopus 로고
    • A simple colorimetric method for the measurement of hydrogen peroxide produced by cells in culture
    • Pick, E., and Y. Keisari. 1980. A simple colorimetric method for the measurement of hydrogen peroxide produced by cells in culture. J. Immunol. Methods 38:161-170.
    • (1980) J. Immunol. Methods , vol.38 , pp. 161-170
    • Pick, E.1    Keisari, Y.2
  • 37
    • 0030789583 scopus 로고    scopus 로고
    • Selection of optimum laboratory tests for the identification of Moraxella catarrhalis
    • Singh, S., K. M. Cisera, J. D. Turnidge, and E. G. Russell. 1997. Selection of optimum laboratory tests for the identification of Moraxella catarrhalis. Pathology 29:206-208.
    • (1997) Pathology , vol.29 , pp. 206-208
    • Singh, S.1    Cisera, K.M.2    Turnidge, J.D.3    Russell, E.G.4
  • 40
    • 0014263775 scopus 로고
    • Evidence suggesting importance of role of interbacterial inhibition in maintaining balance of normal flora
    • Sprunt, K., and W. Redman. 1968. Evidence suggesting importance of role of interbacterial inhibition in maintaining balance of normal flora. Ann. Intern. Med. 68:579-590.
    • (1968) Ann. Intern. Med. , vol.68 , pp. 579-590
    • Sprunt, K.1    Redman, W.2
  • 41
    • 0042643194 scopus 로고
    • The inhibitory action of saliva on the diphtheria bacillus: Hydrogen peroxide, the inhibitory agent produced by salivary streptococci
    • Thompson, R., and A. Johnson. 1951. The inhibitory action of saliva on the diphtheria bacillus: hydrogen peroxide, the inhibitory agent produced by salivary streptococci. J. Infect. Dis. 88:81-85.
    • (1951) J. Infect. Dis. , vol.88 , pp. 81-85
    • Thompson, R.1    Johnson, A.2
  • 42
    • 0028307194 scopus 로고
    • Phase variation in pneumococcal opacity: Relationship between colonial morphology and nasopharyngeal colonization
    • Weiser, J. N., R. Austrian, P. K. Sreenivasan, and H. R. Masure. 1994. Phase variation in pneumococcal opacity: relationship between colonial morphology and nasopharyngeal colonization. Infect. Immun. 62:2582-2589.
    • (1994) Infect. Immun. , vol.62 , pp. 2582-2589
    • Weiser, J.N.1    Austrian, R.2    Sreenivasan, P.K.3    Masure, H.R.4
  • 43
    • 0029096438 scopus 로고
    • Identification and characterization of a cell envelope protein of Haemophilus influenzae contributing to phase variation in colony opacity and nasopharyngeal colonization
    • Weiser, J. N., S. T. H. Chong, D. Greenberg, and W. Fong. 1995. Identification and characterization of a cell envelope protein of Haemophilus influenzae contributing to phase variation in colony opacity and nasopharyngeal colonization. Mol. Microbiol. 17:555-564.
    • (1995) Mol. Microbiol. , vol.17 , pp. 555-564
    • Weiser, J.N.1    Chong, S.T.H.2    Greenberg, D.3    Fong, W.4
  • 44
    • 0024465134 scopus 로고
    • The molecular mechanism of phase variation of H, influenzae lipopolysaccharide
    • Weiser, J. N., J. M. Love, and E. R. Moxon. 1989. The molecular mechanism of phase variation of H, influenzae lipopolysaccharide. Cell 59:657-665.
    • (1989) Cell , vol.59 , pp. 657-665
    • Weiser, J.N.1    Love, J.M.2    Moxon, E.R.3
  • 45
    • 0032536372 scopus 로고    scopus 로고
    • Phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae contributes to persistence in the respiratory tract and sensitivity to serum killing mediated by C-reactive protein
    • Weiser, J. N., N. Pan, K. L. McGowan, D. Musher, A. Martin, and J. C. Richards. 1998. Phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae contributes to persistence in the respiratory tract and sensitivity to serum killing mediated by C-reactive protein. J. Exp. Med. 187:631-640.
    • (1998) J. Exp. Med. , vol.187 , pp. 631-640
    • Weiser, J.N.1    Pan, N.2    McGowan, K.L.3    Musher, D.4    Martin, A.5    Richards, J.C.6
  • 46
    • 0031036365 scopus 로고    scopus 로고
    • Decoration of lipopolysaccaride with phosphorylcholine: A phase-variable characteristic of Haemophilus influenzae
    • Weiser, J. N., M. Shchepetov, and S. T. H. Chong. 1997. Decoration of lipopolysaccaride with phosphorylcholine: a phase-variable characteristic of Haemophilus influenzae. Infect. Immun. 65:943-950.
    • (1997) Infect. Immun. , vol.65 , pp. 943-950
    • Weiser, J.N.1    Shchepetov, M.2    Chong, S.T.H.3
  • 47
    • 36949090933 scopus 로고
    • Possible identity of "lactobacillin" with hydrogen peroxide produced by lactobacilli
    • Wheater, D. M., A. Hirsch, and A. T. R. Mattick. 1952. Possible identity of "lactobacillin" with hydrogen peroxide produced by lactobacilli. Nature 170: 623-624.
    • (1952) Nature , vol.170 , pp. 623-624
    • Wheater, D.M.1    Hirsch, A.2    Mattick, A.T.R.3
  • 48
    • 0001307325 scopus 로고
    • Hemin biosynthesis in Haemophilus
    • White, D. C., and G. S. White. 1963. Hemin biosynthesis in Haemophilus. J. Bacteriol. 85:842-850.
    • (1963) J. Bacteriol. , vol.85 , pp. 842-850
    • White, D.C.1    White, G.S.2
  • 49
    • 0002839521 scopus 로고
    • Hydrogen peroxide formation and catalase activity in the lactic acid bacteria
    • Whittenbury, R. 1964. Hydrogen peroxide formation and catalase activity in the lactic acid bacteria. J. Gen. Microbiol. 35:13-26.
    • (1964) J. Gen. Microbiol. , vol.35 , pp. 13-26
    • Whittenbury, R.1
  • 50
    • 0023823480 scopus 로고
    • Partial characterisation of the inhibitory substances produced by Streptococcus oralis and related species
    • Wilcox, M. D. P., and D. B. Drucker. 1988. Partial characterisation of the inhibitory substances produced by Streptococcus oralis and related species. Microbios 55:135-145.
    • (1988) Microbios , vol.55 , pp. 135-145
    • Wilcox, M.D.P.1    Drucker, D.B.2
  • 51
    • 0031925094 scopus 로고    scopus 로고
    • Generation and properties of a Streptococcus pneumoniae mutant which does not require choline or analogs for growth
    • Yother, J., K. Leopold, J. White, and W. Fischer. 1998. Generation and properties of a Streptococcus pneumoniae mutant which does not require choline or analogs for growth. J. Bacteriol. 180:2093-2101.
    • (1998) J. Bacteriol. , vol.180 , pp. 2093-2101
    • Yother, J.1    Leopold, K.2    White, J.3    Fischer, W.4
  • 52
    • 0028172996 scopus 로고
    • 2-producing lactobacilli on Neisseria gonorrhoeae growth and catalase activity
    • 2-producing lactobacilli on Neisseria gonorrhoeae growth and catalase activity. J. Infect. Dis. 170:1209-1215.
    • (1994) J. Infect. Dis. , vol.170 , pp. 1209-1215
    • Zheng, H.Y.1    Alcorn, T.M.2    Cohen, M.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.